EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
1.17.2.3 | formate + ferri-Ssc |
Ssc i.e. split-Soret cytochrome |
Desulfovibrio desulfuricans |
CO2 + ferro-Ssc |
- |
? |
1.17.2.3 | formate + ferri-TpIc3 |
TpIc3 i.e. tetraheme type I cytochrome c3 |
Desulfovibrio desulfuricans |
CO2 + ferro-TpIc3 |
- |
? |
1.17.2.3 | formate + ferricytochrome c-553 |
- |
Desulfovibrio vulgaris |
CO2 + ferrocytochrome c-553 |
- |
ir |
1.17.2.3 | formate + ferricytochrome c-553 |
yeast cytochrome c, ferricyanide and phenazine methosulfate can act as acceptors, not: NAD+, NADP+, FAD, FMN, cytochrome c3 |
Desulfovibrio vulgaris |
CO2 + ferrocytochrome c-553 |
- |
ir |
1.17.2.3 | formate + ferricytochrome c-553 |
the FDH2C subunit is needed for the reduction of ferricytochrome c-553 |
Desulfovibrio vulgaris |
CO2 + ferrocytochrome c-553 |
- |
? |
1.17.2.3 | formate + ferricytochrome c-553 |
highest rate for reduction by FdhABC3, much higher than that observed with other cytochromes i.e. TpIc3, Ssc, NhcA or Dsr |
Desulfovibrio desulfuricans |
CO2 + ferrocytochrome c-553 |
- |
? |
1.17.2.3 | formate + ferricytochrome c-553 |
- |
Desulfovibrio vulgaris G200 |
CO2 + ferrocytochrome c-553 |
- |
ir |
1.17.2.3 | formate + ferricytochrome c-553 |
the FDH2C subunit is needed for the reduction of ferricytochrome c-553 |
Desulfovibrio vulgaris Hildenborough |
CO2 + ferrocytochrome c-553 |
- |
? |
1.17.2.3 | more |
analysis of the Desulfovibrio desulfuricans ATCC 27774 genome shows that no cytochrome c-553 is present in this organism, thus the cytochrome c-553 is not a physiological redox partner of FDH and because cytochrome c-553 has a very high redox potentials in contrast to the low redox potentials of TpIc3 it is more likely that TpIc3 is involved in electron transfer from formate |
Desulfovibrio desulfuricans |
? |
- |
? |